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| Other Authors: | |
| Format: | Thesis |
| Language: | English |
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Department of Chemistry
2014
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| _version_ | 1867611302841548800 |
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| access_status_str | Open Access |
| author | Stone, Shane Ramsay |
| author2 | Jackson, Graham Ellis |
| author_browse | Jackson, Graham Ellis Stone, Shane Ramsay |
| author_facet | Jackson, Graham Ellis Stone, Shane Ramsay |
| author_sort | Stone, Shane Ramsay |
| collection | Thesis |
| description | Word processed copy. |
| format | Thesis |
| id | oai:open.uct.ac.za:11427/6289 |
| institution | University of Cape Town (South Africa) |
| language | eng |
| license_str | Not specified — see source repository |
| provenance_str_mv | Harvested via OAI-PMH from UCTD — University of Cape Town Open Access Repository |
| publishDate | 2014 |
| publishDateRange | 2014 |
| publishDateSort | 2014 |
| publisher | Department of Chemistry |
| publisherStr | Department of Chemistry |
| record_format | dspace |
| source_str | UCTD — University of Cape Town Open Access Repository |
| spelling | oai:open.uct.ac.za:11427/6289 Structural characterisation of the solution and membrane-associated conformations of human little gastrin and its bioactive fragments by NMR spectroscopy and molecular modelling Stone, Shane Ramsay Jackson, Graham Ellis Chemistry Word processed copy. Includes bibliographical references. The solution studies aimed to determine the conformations of a series of DMSO solubilised gastrin peptides, G-4, [ß-Ala ¹] G-5 and G-17, so as to establish how the configurations of the biologically relevant sequence were related to each other, and to resolve whether they adopted preferred and conserved conformations in solution. Interproton distance restraints were calculated from measured NOe crosspeak intensities for each peptide. 2014-08-13T14:25:47Z 2014-08-13T14:25:47Z 2006 Doctoral Thesis Doctoral PhD http://hdl.handle.net/11427/6289 eng application/pdf Department of Chemistry Faculty of Science University of Cape Town |
| spellingShingle | Chemistry Stone, Shane Ramsay Structural characterisation of the solution and membrane-associated conformations of human little gastrin and its bioactive fragments by NMR spectroscopy and molecular modelling |
| thesis_degree_str | Doctoral |
| title | Structural characterisation of the solution and membrane-associated conformations of human little gastrin and its bioactive fragments by NMR spectroscopy and molecular modelling |
| title_full | Structural characterisation of the solution and membrane-associated conformations of human little gastrin and its bioactive fragments by NMR spectroscopy and molecular modelling |
| title_fullStr | Structural characterisation of the solution and membrane-associated conformations of human little gastrin and its bioactive fragments by NMR spectroscopy and molecular modelling |
| title_full_unstemmed | Structural characterisation of the solution and membrane-associated conformations of human little gastrin and its bioactive fragments by NMR spectroscopy and molecular modelling |
| title_short | Structural characterisation of the solution and membrane-associated conformations of human little gastrin and its bioactive fragments by NMR spectroscopy and molecular modelling |
| title_sort | structural characterisation of the solution and membrane associated conformations of human little gastrin and its bioactive fragments by nmr spectroscopy and molecular modelling |
| topic | Chemistry |
| url | http://hdl.handle.net/11427/6289 |
| work_keys_str_mv | AT stoneshaneramsay structuralcharacterisationofthesolutionandmembraneassociatedconformationsofhumanlittlegastrinanditsbioactivefragmentsbynmrspectroscopyandmolecularmodelling |